Surfactant protein A (SP-A) is a crucial component of the pulmonary innate immune system in the alveolar spaces. SP-A is the major protein constituent of pulmonary surfactant; it is involved in organization of large aggregate surfactant phospholipids lining the alveolar surface and acts as an opsonin for pathogens. SP-A is incorporated in the tubular myelin fraction of pulmonary surfactant that covers the alveolar lining fluid of the distal airway epithelium. The presence of pathogen-derived molecules may trigger reorganization of surfactant lipids and exposure of SP-A to bind pathogens at points of entry on the surfactant interface. Alveolar macrophages in the aqueous hypophase may then patrol areas of disturbance on the surfactant layer binding SP-A-opsonized bacteria, and SP-A has been shown to play an important role in modulating complement receptor-mediated phagocytosis. In this regard, SP-A modulates macrophage phagocytosis and a host of pro- and anti-inflammatory responses that help in eradication of infection first and then resolution of inflammation in vivo. Several macrophage receptors have been implicated in the ability of SP-A to coordinate clearance of pathogens and apoptotic cells and temporal control of inflammation in the lungs. The SP-A receptor SP-R210 was identified as cell surface isoforms of unconventional Myo18A (Yang C. H., et al. (2005) J. Biol. Chem. 280, 34447-34457). The Myo18A gene encodes two alternatively spliced SP-R210 isoforms, SP-R210L and SP-R210S. The longer 230-240-kDa SP-R210L isoform contains an amino-terminal PDZ protein interaction module that is absent from the shorter 210-kDa SP-R210S. SP-R210S is highly expressed in both mature macrophages and in immature monocytic cells. However, SP-R210L is only expressed in mature macrophages. Thus, for a variety of reasons, there is a need to develop novel compositions and methods for selectively targeting/binding the distinct SP-R210 isoforms. The present disclosure meets these and other needs.